The Cochaperone Bag-1L Enhances Androgen Receptor Action via Interaction with the NH₂-Terminal Region of the Receptor

REFERENCES

• Alaiya, A. A., M. Oppermann, J. Langridge, U. Roblick, L. Egevad, S. Brindstedt, M. Hellstrom, S. Linder, T. Bergman, H. Jornvall, and G. Auer. 2001. Identification of proteins in human prostate tumor material by two-dimensional gel electrophoresis and mass spectrometry. Cell Mol. Life Sci. 58: 307–311.
   PubMed Web of Science ®Google Scholar
• Anfinsen, C. B. 1973. Principles that govern the folding of protein chains. Science 181: 223–230.
   PubMed Web of Science ®Google Scholar
• Arbeitman, M. N., and D. S. Hogness. 2000. Molecular chaperones activate the Drosophila ecdysone receptor, an RXR heterodimer. Cell 101: 67–77.
   PubMed Web of Science ®Google Scholar
• Bellmann, K., M. Jäättelä, D. Wissing, V. Burkart, and H. Kolb. 1996. Heat shock protein hsp70 overexpression confers resistance against nitric oxide. FEBS Lett. 391: 185–188.
   PubMedGoogle Scholar
• Bohen, S. P., A. Kralli, and K. R. Yamamoto. 1995. Hold 'em and fold 'em: chaperones and signal transduction. Science 268: 1303–1304.
   PubMed Web of Science ®Google Scholar
• Brehmer, D., S. Rudiger, C. S. Gässler, D. Klostermeier, L. Packschies, J. Reinstein, M. P. Mayer, and B. Bukau. 2001. Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange. Nat. Struct. Biol. 8: 427–432.
   PubMedGoogle Scholar
• Bresnick, E. H., F. C. Dalman, E. R. Sanchez, and W. B. Pratt. 1989. Evidence that the 90-kDa heat shock protein is necessary for the steroid binding conformation of the L cell glucocorticoid receptor. J. Biol. Chem. 264: 4992–4997.
   PubMed Web of Science ®Google Scholar
• Briknarova, K., S. Takayama, L. Brive, M. L. Havert, D. A. Knee, J. Velasco, S. Homma, E. Cabezas, J. Stuart, D. W. Hoyt, A. C. Satterthwait, M. Llinas, J. C. Reed, and K. R. Ely. 2001. Structural analysis of BAG1 cochaperone and its interactions with Hsc70 heat shock protein. Nat. Struct. Biol. 8: 349–352.
   PubMedGoogle Scholar
• Buchner, J. 1999. Hsp90 & Co.—a holding for folding. Trends Biochem. Sci. 24: 136–141.
   PubMed Web of Science ®Google Scholar
• Cato, A. C., and S. Mink. 2001. BAG-1 family of cochaperones in the modulation of nuclear receptor action. J. Steroid Biochem. Mol. Biol. 78: 379–388.
   PubMed Web of Science ®Google Scholar
• Cornford, P. A., A. R. Dodson, K. F. Parsons, A. D. Desmond, A. Woolfenden, M. Fordham, J. P. Neoptolemos, Y. Ke, and C. S. Foster. 2000. Heat shock protein expression independently predicts clinical outcome in prostate cancer. Cancer Res. 60: 7099–7105.
   PubMed Web of Science ®Google Scholar
• Crocoll, A., M. Blum, and A. C. Cato. 2000. Isoform-specific expression of BAG-1 in mouse development. Mech. Dev. 91: 355–359.
   PubMedGoogle Scholar
• Dittmar, K. D., and W. B. Pratt. 1997. Folding of the glucocorticoid receptor by the reconstituted Hsp90-based chaperone machinery. The initial hsp90.p60.hsp70-dependent step is sufficient for creating the steroid binding conformation. J. Biol. Chem. 272: 13047–13054.
   PubMedGoogle Scholar
• Freeman, B. C., S. J. Felts, D. O. Toft, and K. R. Yamamoto. 2000. The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies. Genes Dev. 14: 422–434.
   PubMed Web of Science ®Google Scholar
• Freeman, B. C., and K. R. Yamamoto. 2001. Continuous recycling: a mechanism for modulatory signal transduction. Trends Biochem. Sci. 26: 285–290.
   PubMed Web of Science ®Google Scholar
• Freeman, B. C., and K. R. Yamamoto. 2002. Disassembly of transcriptional regulatory complexes by molecular chaperones. Science 296: 2232–2235.
   PubMed Web of Science ®Google Scholar
• Froesch, B. A., S. Takayama, and J. C. Reed. 1998. BAG-1L protein enhances androgen receptor function. J. Biol. Chem. 273: 11660–11666.
   PubMed Web of Science ®Google Scholar
• Frydman, J., and J. Hühfeld. 1997. Chaperones get in touch: the Hip-Hop connection. Trends Biochem. Sci. 22: 87–92.
   PubMed Web of Science ®Google Scholar
• Gast, A., J. Schneikert, and A. C. Cato. 1998. N-terminal sequences of the human androgen receptor in DNA binding and transrepressing functions. J. Steroid Biochem. Mol. Biol. 65: 117–123.
   PubMedGoogle Scholar
• He, B., J. A. Kemppainen, J. J. Voegel, H. Gronemeyer, and E. M. Wilson. 1999. Activation function 2 in the human androgen receptor ligand binding domain mediates interdomain communication with the NH(2)-terminal domain. J. Biol. Chem. 274: 37219–37225.
   PubMed Web of Science ®Google Scholar
• He, B., J. A. Kemppainen, and E. M. Wilson. 2000. FXXLF and WXXLF sequences mediate the NH2-terminal interaction with the ligand binding domain of the androgen receptor. J. Biol. Chem. 275: 22986–22994.
   PubMed Web of Science ®Google Scholar
• Herscovics, A., J. Schneikert, A. Athanassiadis, and K. W. Moremen. 1994. Isolation of a mouse Golgi mannosidase cDNA, a member of a gene family conserved from yeast to mammals. J. Biol. Chem. 269: 9864–9871.
   PubMedGoogle Scholar
• Hühfeld, J. 1998. Regulation of the heat shock conjugate Hsc70 in the mammalian cell: the characterization of the anti-apoptotic protein BAG-1 provides novel insights. Biol. Chem. 379: 269–274.
   PubMedGoogle Scholar
• Jäättelä, M., D. Wissing, P. A. Bauer, and G. C. Li. 1992. Major heat shock protein hsp70 protects tumor cells from tumor necrosis factor cytotoxicity. EMBO J. 11: 3507–3512.
   PubMed Web of Science ®Google Scholar
• Jenster, G., H. A. van der Korput, J. Trapman, and A. O. Brinkmann. 1995. Identification of two transcription activation units in the N-terminal domain of the human androgen receptor. J. Biol. Chem. 270: 7341–7346.
   PubMed Web of Science ®Google Scholar
• Knee, D. A., B. A. Froesch, U. Nuber, S. Takayama, and J. C. Reed. 2001. Structure-function analysis of Bag1 proteins. Effects on androgen receptor transcriptional activity. J. Biol. Chem. 276: 12718–12724.
   PubMedGoogle Scholar
• Kullmann, M., J. Schneikert, J. Moll, S. Heck, M. Zeiner, U. Gehring, and A. C. Cato. 1998. RAP46 is a negative regulator of glucocorticoid receptor action and hormone-induced apoptosis. J. Biol. Chem. 273: 14620–14625.
   PubMed Web of Science ®Google Scholar
• Langley, E., Z. X. Zhou, and E. M. Wilson. 1995. Evidence for an anti-parallel orientation of the ligand-activated human androgen receptor dimer. J. Biol. Chem. 270: 29983–29990.
   PubMed Web of Science ®Google Scholar
• Milarski, K. L., and R. I. Morimoto. 1989. Mutational analysis of the human HSP70 protein: distinct domains for nucleolar localization and adenosine triphosphate binding. J. Cell Biol. 109: 1947–1962.
   PubMed Web of Science ®Google Scholar
• Mink, S., B. Haenig, and K. H. Klempnauer. 1997. Interaction and functional collaboration of p300 and C/EBPbeta. Mol. Cell. Biol. 17: 6609–6617.
   PubMed Web of Science ®Google Scholar
• Mink, S., U. Kerber, and K. H. Klempnauer. 1996. Interaction of C/EBPbeta and v-Myb is required for synergistic activation of the mim-1 gene. Mol. Cell. Biol. 16: 1316–1325.
   PubMedGoogle Scholar
• Morimoto, R. I. 2002. Dynamic remodeling of transcription complexes by molecular chaperones. Cell 110: 281–284.
   PubMedGoogle Scholar
• Niyaz, Y., M. Zeiner, and U. Gehring. 2001. Transcriptional activation by the human Hsp70-associating protein Hap50. J. Cell Sci. 114: 1839–1845.
   PubMedGoogle Scholar
• Peterziel, H., S. Mink, A. Schonert, M. Becker, H. Klocker, and A. C. B. Cato. 1999. Rapid signalling by androgen receptor in prostate cancer cells. Oncogene 18: 6322–6329.
   PubMed Web of Science ®Google Scholar
• Schneikert, J., S. Hübner, G. Langer, T. Petri, M. Jäättelä, J. Reed, and A. C. Cato. 2000. Hsp70-RAP46 interaction in downregulation of DNA binding by glucocorticoid receptor. EMBO J. 19: 6508–6516.
   PubMedGoogle Scholar
• Schneikert, J., S. Hübner, E. Martin, and A. C. Cato. 1999. A nuclear action of the eukaryotic cochaperone RAP46 in downregulation of glucocorticoid receptor activity. J. Cell Biol. 146: 929–940.
   PubMedGoogle Scholar
• Shang, Y., M. Myers, and M. Brown. 2002. Formation of the androgen receptor transcription complex. Mol. Cell 9: 601–610.
   PubMed Web of Science ®Google Scholar
• Smith, D. F., and D. O. Toft. 1993. Steroid receptors and their associated proteins. Mol. Endocrinol. 7: 4–11.
   PubMed Web of Science ®Google Scholar
• Sondermann, H., C. Scheufler, C. Schneider, J. Hühfeld, F. U. Hartl, and I. Moarefi. 2001. Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors. Science 291: 1553–1557.
   PubMed Web of Science ®Google Scholar
• Sramkoski, R. M., T. G. Pretlow, Jr., J. M. Giaconia, T. P. Pretlow., S. Schwartz, M. S. Sy, S. R. Marengo, J. S. Rhim, D. Zhang and J. W. Jacobberger. 1999. A new human prostate carcinoma cell line, 22Rv1. In Vitro Cell Dev. Biol. Anim. 35: 403–409.
   Google Scholar
• Takayama, S., and J. C. Reed. 2001. Molecular chaperone targeting and regulation by BAG family proteins. Nat. Cell Biol. 3: E237–E241.
   PubMed Web of Science ®Google Scholar
• Zeiner, M., M. Gebauer, and U. Gehring. 1997. Mammalian protein RAP46: an interaction partner and modulator of 70 kDa heat shock proteins. EMBO J. 16: 5483–5490.
   PubMedGoogle Scholar